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RIPK1-DD has a role in mediating RIPK1 dimerization and activation of its kinase activity during necroptosis and RIPK1-dependent apoptosis
We further identified this underlying mechanism also involved a PPARgamma (show PPARG Proteins)-induced ANXA1 (show ANXA1 Proteins)-dependent autoubiquitination of cIAP1 (show BIRC2 Proteins), the direct E3 ligase of RIP1 (show UQCRFS1 Proteins), shifting cIAP1 (show BIRC2 Proteins) toward proteosomal degradation..our study provides first insight for the suitability of using drug-induced expression of ANXA1 (show ANXA1 Proteins) as a new player in RIP1 (show UQCRFS1 Proteins)-induced death machinery in triple-negative breast cancer
data suggest that artesunate could induce RIP1-dependent cell death in human renal carcinoma.
RIP1 (show UQCRFS1 Proteins) has a role in CD40 (show CD40 Proteins)-mediated activation of caspase-8 (show CASP8 Proteins), which in turn leads to induction of apoptosis
High RIPK1 expression is associated with Alzheimer's disease.
These data represent the first report of decreased RIPK1 expression in neutrophils of Systemic Lupus Erythematosus patients and imply that RIPK1 may be involved in neutrophil death and neutrophil extracellular traps formation.
Data indicate that receptor (TNFRSF)-interacting serine-threonine kinase 1 (RIPK1) polymorphism is a prognostic biomarker for tumor development and survival of hepatocellular carcinoma (HCC (show FAM126A Proteins)) patients after hepatectomy.
we found that ORF3 protein downregulates TLR3 (show TLR3 Proteins)-mediated NF-kappaB (show NFKB1 Proteins) signaling via TRADD (show TRADD Proteins) and RIP1 (show UQCRFS1 Proteins). Our findings provide a new perspective on the cellular response in HEV infection and expand our understanding of the molecular mechanisms of Hepatitis E virus (HEV) pathogenesis in innate immunity.
Existence of a kinase-independent role of nuclear RIPK1 in the regulation of PARP1 (show PARP1 Proteins).
Study identify and quantify over 8,000 phosphorylated peptides, among which are numerous known sites in the TNF (show TNF Proteins)-RSC, NFkappaB (show NFKB1 Proteins), and MAP kinase (show MAPK1 Proteins) signaling systems. Functional analysis of S320 phosphorylation in RIPK1 demonstrates a role for this event in suppressing its kinase activity, association with CASPASE-8 (show CASP8 Proteins) and FADD (show FADD Proteins) proteins, and subsequent necrotic cell death during inflammatory TNFalpha (show TNF Proteins) stimulation.
We show that inflammation and autoimmunity are prevented upon expression of kinase inactive RIPK1 or deletion of RIPK3 (show RIPK3 Proteins) or MLKL. We provide evidence that the inflammation is not driven by microbial ligands, but depends on the release of danger-associated molecular patterns and MyD88 (show MYD88 Proteins)-dependent signaling.
RIPK1 kinase activity mediates TWEAK (show TNFSF12 Proteins)-induced apoptosis.
The authors report here that male reproductive organs of both Ripk3 (show RIPK3 Proteins)- and Mlkl-knockout mice retain 'youthful' morphology and function into advanced age, while those of age-matched wild-type mice deteriorate. Feeding of wild-type mice with an RIPK1 inhibitor prior to the normal onset of age-related changes in their reproductive organs blocked the appearance of signs of aging.
Pull down experiments with biotinylated Sorafenib show that it binds independently RIPK1, RIPK3 (show RIPK3 Proteins) and MLKL. Moreover, it inhibits RIPK1 and RIPK3 (show RIPK3 Proteins) kinase activity. In vivo Sorafenib protects against TNF (show TNF Proteins)-induced systemic inflammatory response syndrome (SIRS) and renal ischemia-reperfusion injury (IRI).
The study provides genetic evidence that different RIP1 kinase inactive mutations have distinct impacts on the embryogenesis of Fadd-deficient mice.
Excessive death of hepatocytes is a characteristic of liver injury. A new programmed cell death pathway has been described involving upstream death ligands such as TNF (show TNF Proteins) and downstream kinases such as RIPK1.
TNFalpha (show TNF Proteins)-induced phosphorylation of RIPK1 in the intermediate domain by TAK1 (show NR2C2 Proteins) plays a key role in regulating the decision between three distinct mechanisms of cell death: necroptosis, RIPK1-independent and dependent apoptosis.
K45 mediated kinase activity of RIPK1 is not only important for necroptosis but it also has a key role in promoting cytokine signaling and host response to inflammatory stimuli.
Interaction of xFADD and xRIP1 induced synergistic activation of JNK (show MAPK8 Proteins) and NF-kappaB (show NFKB1 Proteins).
Serine-threonine kinase which transduces inflammatory and cell-death signals (necroptosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necroptosis-inducing complex.
, cell death protein RIP
, receptor interacting protein
, receptor-interacting protein 1
, receptor-interacting serine/threonine-protein kinase 1
, serine/threonine-protein kinase RIP
, receptor (TNFRSF)-interacting serine-threonine kinase 1
, receptor interacting serine/threonine kinase 1 L homeolog
, receptor-interacting protein 1 beta